3k92 - Revision history

OCA at 08:29, 20 March 2024

2024-03-20T08:29:26Z

←Older revision		Revision as of 08:29, 20 March 2024
Line 3:		Line 3:
	<StructureSection load='3k92' size='340' side='right'caption='[[3k92]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='3k92' size='340' side='right'caption='[[3k92]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3k92]] is a 6 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~"vibrio_subtilis"_ehrenberg_1835 "vibrio~~ subtilis~~" ehrenberg 1835~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K92 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=3K92 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3k92]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K92 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3K92 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.3Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~>[[3k8z\|3k8z]]</td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
-	~~<tr~~ id~~='activity'><td class~~="~~sblockLbl~~"><~~b>Activity:</b></td><td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>~~[http://en.wikipedia.org/wiki/Glutamate_dehydrogenase Glutamate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.1.2 1.4.1.2]~~ </~~span~~></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3k92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k92 OCA], [https://pdbe.org/3k92 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3k92 RCSB], [https://www.ebi.ac.uk/pdbsum/3k92 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3k92 ProSAT]</span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=3k92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k92 OCA], [~~http~~://pdbe.org/3k92 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3k92 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3k92 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3k92 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/DHE2_BACSU DHE2_BACSU]] Devoted to catabolic function of glutamate (and other amino acids of the glutamate family) utilization as sole nitrogen source. It is not involved in anabolic function of glutamate biosynthesis since B.subtilis possesses only one route of glutamate biosynthesis from ammonia, catalyzed by glutamate synthase. RocG is unable to utilize glutamate or glutamine as sole carbon source and to synthesize glutamate, but it is involved in the utilization of arginine, and proline as carbon or nitrogen source. The catabolic RocG is essential for controlling gltAB expression via an inhibitory interactions with the transcriptional regulator GltC in response to the availability of sugars.<ref>PMID:9829940</ref> <ref>PMID:17183217</ref> <ref>PMID:18326565</ref>	+	[https://www.uniprot.org/uniprot/DHE2_BACSU DHE2_BACSU] Devoted to catabolic function of glutamate (and other amino acids of the glutamate family) utilization as sole nitrogen source. It is not involved in anabolic function of glutamate biosynthesis since B.subtilis possesses only one route of glutamate biosynthesis from ammonia, catalyzed by glutamate synthase. RocG is unable to utilize glutamate or glutamine as sole carbon source and to synthesize glutamate, but it is involved in the utilization of arginine, and proline as carbon or nitrogen source. The catabolic RocG is essential for controlling gltAB expression via an inhibitory interactions with the transcriptional regulator GltC in response to the availability of sugars.<ref>PMID:9829940</ref> <ref>PMID:17183217</ref> <ref>PMID:18326565</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 21:		Line 20:
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3k92 ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3k92 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Any signal transduction requires communication between a sensory component and an effector. Some enzymes engage in signal perception and transduction, as well as in catalysis, and these proteins are known as "trigger" enzymes. In this report, we detail the trigger properties of RocG, the glutamate dehydrogenase of Bacillus subtilis. RocG not only deaminates the key metabolite glutamate to form alpha-ketoglutarate but also interacts directly with GltC, a LysR-type transcription factor that regulates glutamate biosynthesis from alpha-ketoglutarate, thus linking the two metabolic pathways. We have isolated mutants of RocG that separate the two functions. Several mutations resulted in permanent inactivation of GltC as long as a source of glutamate was present. These RocG proteins have lost their ability to catabolize glutamate due to a strongly reduced affinity for glutamate. The second class of mutants is exemplified by the replacement of aspartate residue 122 by asparagine. This mutant protein has retained enzymatic activity but has lost the ability to control the activity of GltC. Crystal structures of glutamate dehydrogenases that permit a molecular explanation of the properties of the various mutants are presented. Specifically, we may propose that D122N replacement affects the surface of RocG. Our data provide evidence for a correlation between the enzymatic activity of RocG and its ability to inactivate GltC, and thus give insights into the mechanism that couples the enzymatic activity of a trigger enzyme to its regulatory function.
-
-	Functional dissection of a trigger enzyme: mutations of the bacillus subtilis glutamate dehydrogenase RocG that affect differentially its catalytic activity and regulatory properties.,Gunka K, Newman JA, Commichau FM, Herzberg C, Rodrigues C, Hewitt L, Lewis RJ, Stulke J J Mol Biol. 2010 Jul 23;400(4):815-27. Epub 2010 May 31. PMID:20630473<ref>PMID:20630473</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 3k92" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 37:		Line 27:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Vibrio~~ subtilis ~~ehrenberg 1835]]~~	+	[[Category: Bacillus subtilis]]
-	~~[[Category: Glutamate dehydrogenase~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Commichau~~, F M~~]]	+	[[Category: Commichau FM]]
-	[[Category: Gunka, K]]	+	[[Category: Gunka K]]
-	[[Category: Herzberg, C]]	+	[[Category: Herzberg C]]
-	[[Category: Hewitt, L]]	+	[[Category: Hewitt L]]
-	[[Category: Lewis~~, R J~~]]	+	[[Category: Lewis RJ]]
-	[[Category: Newman~~, J A~~]]	+	[[Category: Newman JA]]
-	[[Category: Rodrigues, C]]	+	[[Category: Rodrigues C]]
-	[[Category: Stulke, J]]	+	[[Category: Stulke J]]
-	~~[[Category: Nad]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Rocg~~]]	+

OCA at 07:00, 7 October 2020

2020-10-07T07:00:53Z

←Older revision		Revision as of 07:00, 7 October 2020
Line 1:		Line 1:

	==Crystal structure of a E93K mutant of the majour Bacillus subtilis glutamate dehydrogenase RocG==		==Crystal structure of a E93K mutant of the majour Bacillus subtilis glutamate dehydrogenase RocG==
-	<StructureSection load='3k92' size='340' side='right' caption='[[3k92]], [[Resolution\|resolution]] 2.30Å' scene=''>	+	<StructureSection load='3k92' size='340' side='right'caption='[[3k92]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3k92]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K92 OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3K92 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3k92]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K92 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3K92 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3k8z\|3k8z]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3k8z\|3k8z]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate_dehydrogenase Glutamate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.1.2 1.4.1.2] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate_dehydrogenase Glutamate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.1.2 1.4.1.2] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3k92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k92 OCA], [http://pdbe.org/3k92 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3k92 RCSB], [http://www.ebi.ac.uk/pdbsum/3k92 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3k92 ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3k92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k92 OCA], [http://pdbe.org/3k92 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3k92 RCSB], [http://www.ebi.ac.uk/pdbsum/3k92 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3k92 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 32:		Line 32:

	==See Also==		==See Also==
-	*[[Glutamate dehydrogenase\|Glutamate dehydrogenase]]	+	*[[Glutamate dehydrogenase 3D structures\|Glutamate dehydrogenase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 39:		Line 39:
	[[Category: Vibrio subtilis ehrenberg 1835]]		[[Category: Vibrio subtilis ehrenberg 1835]]
	[[Category: Glutamate dehydrogenase]]		[[Category: Glutamate dehydrogenase]]
		+	[[Category: Large Structures]]
	[[Category: Commichau, F M]]		[[Category: Commichau, F M]]
	[[Category: Gunka, K]]		[[Category: Gunka, K]]

OCA at 09:33, 26 December 2018

2018-12-26T09:33:51Z

←Older revision		Revision as of 09:33, 26 December 2018
Line 3:		Line 3:
	<StructureSection load='3k92' size='340' side='right' caption='[[3k92]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='3k92' size='340' side='right' caption='[[3k92]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3k92]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"~~bacillus_globigii~~"~~_migula_1900~~ "~~bacillus globigii~~" ~~migula 1900~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K92 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3K92 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3k92]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K92 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3K92 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3k8z\|3k8z]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3k8z\|3k8z]]</td></tr>
Line 15:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k9/3k92_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k9/3k92_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 37:		Line 37:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Bacillus globigii migula 1900~~]]	+	[[Category: Vibrio subtilis ehrenberg 1835]]
	[[Category: Glutamate dehydrogenase]]		[[Category: Glutamate dehydrogenase]]
	[[Category: Commichau, F M]]		[[Category: Commichau, F M]]

OCA at 20:47, 4 August 2016

2016-08-04T20:47:52Z

←Older revision		Revision as of 20:47, 4 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of a E93K mutant of the majour Bacillus subtilis glutamate dehydrogenase RocG==		==Crystal structure of a E93K mutant of the majour Bacillus subtilis glutamate dehydrogenase RocG==
	<StructureSection load='3k92' size='340' side='right' caption='[[3k92]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='3k92' size='340' side='right' caption='[[3k92]], [[Resolution\|resolution]] 2.30Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3k8z\|3k8z]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3k8z\|3k8z]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate_dehydrogenase Glutamate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.1.2 1.4.1.2] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate_dehydrogenase Glutamate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.1.2 1.4.1.2] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3k92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k92 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3k92 RCSB], [http://www.ebi.ac.uk/pdbsum/3k92 PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3k92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k92 OCA], [http://pdbe.org/3k92 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3k92 RCSB], [http://www.ebi.ac.uk/pdbsum/3k92 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3k92 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3k92 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 28:		Line 29:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 3k92" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 19:30, 24 December 2014

2014-12-24T19:30:46Z

←Older revision		Revision as of 19:30, 24 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3k92\| PDB=3k92 \| SCENE= }}~~	+	==Crystal structure of a E93K mutant of the majour Bacillus subtilis glutamate dehydrogenase RocG==
-	===Crystal structure of a E93K mutant of the majour Bacillus subtilis glutamate dehydrogenase RocG===	+	<StructureSection load='3k92' size='340' side='right' caption='[[3k92]], [[Resolution\|resolution]] 2.30Å' scene=''>
-	~~{{ABSTRACT_PUBMED_20630473}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[3k92]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K92 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3K92 FirstGlance]. <br>
-	==Function==	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3k8z\|3k8z]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate_dehydrogenase Glutamate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.1.2 1.4.1.2] </span></td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3k92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k92 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3k92 RCSB], [http://www.ebi.ac.uk/pdbsum/3k92 PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
	[[http://www.uniprot.org/uniprot/DHE2_BACSU DHE2_BACSU]] Devoted to catabolic function of glutamate (and other amino acids of the glutamate family) utilization as sole nitrogen source. It is not involved in anabolic function of glutamate biosynthesis since B.subtilis possesses only one route of glutamate biosynthesis from ammonia, catalyzed by glutamate synthase. RocG is unable to utilize glutamate or glutamine as sole carbon source and to synthesize glutamate, but it is involved in the utilization of arginine, and proline as carbon or nitrogen source. The catabolic RocG is essential for controlling gltAB expression via an inhibitory interactions with the transcriptional regulator GltC in response to the availability of sugars.<ref>PMID:9829940</ref> <ref>PMID:17183217</ref> <ref>PMID:18326565</ref>		[[http://www.uniprot.org/uniprot/DHE2_BACSU DHE2_BACSU]] Devoted to catabolic function of glutamate (and other amino acids of the glutamate family) utilization as sole nitrogen source. It is not involved in anabolic function of glutamate biosynthesis since B.subtilis possesses only one route of glutamate biosynthesis from ammonia, catalyzed by glutamate synthase. RocG is unable to utilize glutamate or glutamine as sole carbon source and to synthesize glutamate, but it is involved in the utilization of arginine, and proline as carbon or nitrogen source. The catabolic RocG is essential for controlling gltAB expression via an inhibitory interactions with the transcriptional regulator GltC in response to the availability of sugars.<ref>PMID:9829940</ref> <ref>PMID:17183217</ref> <ref>PMID:18326565</ref>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k9/3k92_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Any signal transduction requires communication between a sensory component and an effector. Some enzymes engage in signal perception and transduction, as well as in catalysis, and these proteins are known as "trigger" enzymes. In this report, we detail the trigger properties of RocG, the glutamate dehydrogenase of Bacillus subtilis. RocG not only deaminates the key metabolite glutamate to form alpha-ketoglutarate but also interacts directly with GltC, a LysR-type transcription factor that regulates glutamate biosynthesis from alpha-ketoglutarate, thus linking the two metabolic pathways. We have isolated mutants of RocG that separate the two functions. Several mutations resulted in permanent inactivation of GltC as long as a source of glutamate was present. These RocG proteins have lost their ability to catabolize glutamate due to a strongly reduced affinity for glutamate. The second class of mutants is exemplified by the replacement of aspartate residue 122 by asparagine. This mutant protein has retained enzymatic activity but has lost the ability to control the activity of GltC. Crystal structures of glutamate dehydrogenases that permit a molecular explanation of the properties of the various mutants are presented. Specifically, we may propose that D122N replacement affects the surface of RocG. Our data provide evidence for a correlation between the enzymatic activity of RocG and its ability to inactivate GltC, and thus give insights into the mechanism that couples the enzymatic activity of a trigger enzyme to its regulatory function.

-	~~==About this Structure==~~	+	Functional dissection of a trigger enzyme: mutations of the bacillus subtilis glutamate dehydrogenase RocG that affect differentially its catalytic activity and regulatory properties.,Gunka K, Newman JA, Commichau FM, Herzberg C, Rodrigues C, Hewitt L, Lewis RJ, Stulke J J Mol Biol. 2010 Jul 23;400(4):815-27. Epub 2010 May 31. PMID:20630473<ref>PMID:20630473</ref>
-	~~[[3k92]] is~~ a ~~6 chain structure with sequence from [http~~:~~//en~~.~~wikipedia~~.~~org/wiki/"bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900]~~. ~~Full crystallographic information is available from [http~~://~~oca~~.~~weizmann~~.ac.il/~~oca-bin/ocashort?id=3K92 OCA].~~	+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

	==See Also==		==See Also==
	*[[Glutamate dehydrogenase\|Glutamate dehydrogenase]]		*[[Glutamate dehydrogenase\|Glutamate dehydrogenase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:020630473</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Bacillus globigii migula 1900]]		[[Category: Bacillus globigii migula 1900]]
	[[Category: Glutamate dehydrogenase]]		[[Category: Glutamate dehydrogenase]]
-	[[Category: Commichau, F M.]]	+	[[Category: Commichau, F M]]
-	[[Category: Gunka, K.]]	+	[[Category: Gunka, K]]
-	[[Category: Herzberg, C.]]	+	[[Category: Herzberg, C]]
-	[[Category: Hewitt, L.]]	+	[[Category: Hewitt, L]]
-	[[Category: Lewis, R J.]]	+	[[Category: Lewis, R J]]
-	[[Category: Newman, J A.]]	+	[[Category: Newman, J A]]
-	[[Category: Rodrigues, C.]]	+	[[Category: Rodrigues, C]]
-	[[Category: Stulke, J~~.]]~~	+	[[Category: Stulke, J]]
-	~~[[Category: Glutamate dehydrogenase~~]]	+
	[[Category: Nad]]		[[Category: Nad]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
	[[Category: Rocg]]		[[Category: Rocg]]

OCA at 06:01, 22 January 2014

2014-01-22T06:01:07Z

←Older revision		Revision as of 06:01, 22 January 2014
Line 1:		Line 1:
-	[[Image:3k92.png\|left\|200px]]
-
	{{STRUCTURE_3k92\| PDB=3k92 \| SCENE= }}		{{STRUCTURE_3k92\| PDB=3k92 \| SCENE= }}
-
	===Crystal structure of a E93K mutant of the majour Bacillus subtilis glutamate dehydrogenase RocG===		===Crystal structure of a E93K mutant of the majour Bacillus subtilis glutamate dehydrogenase RocG===
		+	{{ABSTRACT_PUBMED_20630473}}

-	~~{{ABSTRACT_PUBMED_020630473}}~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/DHE2_BACSU DHE2_BACSU]] Devoted to catabolic function of glutamate (and other amino acids of the glutamate family) utilization as sole nitrogen source. It is not involved in anabolic function of glutamate biosynthesis since B.subtilis possesses only one route of glutamate biosynthesis from ammonia, catalyzed by glutamate synthase. RocG is unable to utilize glutamate or glutamine as sole carbon source and to synthesize glutamate, but it is involved in the utilization of arginine, and proline as carbon or nitrogen source. The catabolic RocG is essential for controlling gltAB expression via an inhibitory interactions with the transcriptional regulator GltC in response to the availability of sugars.<ref>PMID:9829940</ref> <ref>PMID:17183217</ref> <ref>PMID:18326565</ref>

	==About this Structure==		==About this Structure==
-	[[3k92]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Bacillus_subtilis Bacillus subtilis~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K92 OCA].	+	[[3k92]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K92 OCA].

	==See Also==		==See Also==
Line 14:		Line 13:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:020630473</ref><references group="xtra"/>	+	<ref group="xtra">PMID:020630473</ref><references group="xtra"/><references/>
-	[[Category: Bacillus ~~subtilis~~]]	+	[[Category: Bacillus globigii migula 1900]]
	[[Category: Glutamate dehydrogenase]]		[[Category: Glutamate dehydrogenase]]
	[[Category: Commichau, F M.]]		[[Category: Commichau, F M.]]

OCA at 08:25, 20 October 2012

2012-10-20T08:25:32Z

←Older revision		Revision as of 08:25, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3k92]] is a 6 chain structure ~~of [[Glutamate dehydrogenase]]~~ with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K92 OCA].	+	[[3k92]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K92 OCA].

	==See Also==		==See Also==

OCA: Protected "3k92" [edit=sysop:move=sysop]

2012-07-25T19:29:03Z

Protected "3k92" [edit=sysop:move=sysop]

←Older revision

Revision as of 19:29, 25 July 2012

OCA at 19:29, 25 July 2012

2012-07-25T19:29:01Z

←Older revision		Revision as of 19:29, 25 July 2012
Line 1:		Line 1:
-	~~{{Seed}}~~	+	[[Image:3k92.png\|left\|200px]]
-	[[Image:3k92.~~jpg~~\|left\|200px]]	+

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3k92", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_3k92\| PDB=3k92 \| SCENE= }}		{{STRUCTURE_3k92\| PDB=3k92 \| SCENE= }}

	===Crystal structure of a E93K mutant of the majour Bacillus subtilis glutamate dehydrogenase RocG===		===Crystal structure of a E93K mutant of the majour Bacillus subtilis glutamate dehydrogenase RocG===

		+	{{ABSTRACT_PUBMED_020630473}}

	==About this Structure==		==About this Structure==
-	~~3K92~~ is a 6 ~~chains~~ structure with ~~sequences~~ from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K92 OCA].	+	[[3k92]] is a 6 chain structure of [[Glutamate dehydrogenase]] with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K92 OCA].
		+
		+	==See Also==
		+	*[[Glutamate dehydrogenase\|Glutamate dehydrogenase]]
		+
		+	==Reference==
		+	<ref group="xtra">PMID:020630473</ref><references group="xtra"/>
	[[Category: Bacillus subtilis]]		[[Category: Bacillus subtilis]]
	[[Category: Glutamate dehydrogenase]]		[[Category: Glutamate dehydrogenase]]
Line 29:		Line 29:
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
	[[Category: Rocg]]		[[Category: Rocg]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 2 08:38:25 2010''

OCA at 04:33, 2 June 2010

2010-06-02T04:33:59Z

←Older revision		Revision as of 04:33, 2 June 2010
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{Seed}}
		+	[[Image:3k92.jpg\|left\|200px]]

-	The ~~entry 3k92~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3k92", creates the "Structure Box" on the page.
		+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
		+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
		+	or leave the SCENE parameter empty for the default display.
		+	-->
		+	{{STRUCTURE_3k92\| PDB=3k92 \| SCENE= }}

-	~~Authors: Gunka, K., Newman, J.A., Commichau, F.M., Herzberg, C., Rodrigues, C., Hewitt, L., Lewis, R.J., Stulke, J.~~	+	===Crystal structure of a E93K mutant of the majour Bacillus subtilis glutamate dehydrogenase RocG===

-	Description: Crystal structure of a E93K mutant of the majour Bacillus subtilis glutamate dehydrogenase RocG

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~Dec 23 09~~:21:~~11 2009~~''	+	==About this Structure==
		+	3K92 is a 6 chains structure with sequences from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K92 OCA].
		+	[[Category: Bacillus subtilis]]
		+	[[Category: Glutamate dehydrogenase]]
		+	[[Category: Commichau, F M.]]
		+	[[Category: Gunka, K.]]
		+	[[Category: Herzberg, C.]]
		+	[[Category: Hewitt, L.]]
		+	[[Category: Lewis, R J.]]
		+	[[Category: Newman, J A.]]
		+	[[Category: Rodrigues, C.]]
		+	[[Category: Stulke, J.]]
		+	[[Category: Glutamate dehydrogenase]]
		+	[[Category: Nad]]
		+	[[Category: Oxidoreductase]]
		+	[[Category: Rocg]]
		+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 2 08:38:25 2010''